Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach
TOR proteins, also known as targets of rapamycin, are serine/threonine kinases involved in various signaling pathways that regulate cell growth. The protozoan parasite <i>Giardia lamblia</i> is the causative agent of giardiasis, a neglected infectious disease in humans. In this study, we...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-07-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/15/11992 |
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| author | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra |
| author_facet | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra |
| author_sort | Patricia L. A. Muñoz-Muñoz |
| collection | DOAJ |
| description | TOR proteins, also known as targets of rapamycin, are serine/threonine kinases involved in various signaling pathways that regulate cell growth. The protozoan parasite <i>Giardia lamblia</i> is the causative agent of giardiasis, a neglected infectious disease in humans. In this study, we used a bioinformatics approach to examine the structural features of GTOR, a <i>G. lamblia</i> TOR-like protein, and predict functional associations. Our findings confirmed that it shares significant similarities with functional TOR kinases, including a binding domain for the FKBP-rapamycin complex and a kinase domain resembling that of phosphatidylinositol 3-kinase-related kinases. In addition, it can form multiprotein complexes such as TORC1 and TORC2. These results provide valuable insights into the structure–function relationship of GTOR, highlighting its potential as a molecular target for controlling <i>G. lamblia</i> cell proliferation. Furthermore, our study represents a step toward rational drug design for specific anti-giardiasis therapeutic agents. |
| first_indexed | 2024-03-11T00:26:28Z |
| format | Article |
| id | doaj.art-6ec3d71fe7c6453f9654477556723c7a |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T00:26:28Z |
| publishDate | 2023-07-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-6ec3d71fe7c6453f9654477556723c7a2023-11-18T22:58:54ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-07-0124151199210.3390/ijms241511992Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics ApproachPatricia L. A. Muñoz-Muñoz0Rosa E. Mares-Alejandre1Samuel G. Meléndez-López2Marco A. Ramos-Ibarra3Biotechnology and Biosciences Research Group, School of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, School of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, School of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoBiotechnology and Biosciences Research Group, School of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, MexicoTOR proteins, also known as targets of rapamycin, are serine/threonine kinases involved in various signaling pathways that regulate cell growth. The protozoan parasite <i>Giardia lamblia</i> is the causative agent of giardiasis, a neglected infectious disease in humans. In this study, we used a bioinformatics approach to examine the structural features of GTOR, a <i>G. lamblia</i> TOR-like protein, and predict functional associations. Our findings confirmed that it shares significant similarities with functional TOR kinases, including a binding domain for the FKBP-rapamycin complex and a kinase domain resembling that of phosphatidylinositol 3-kinase-related kinases. In addition, it can form multiprotein complexes such as TORC1 and TORC2. These results provide valuable insights into the structure–function relationship of GTOR, highlighting its potential as a molecular target for controlling <i>G. lamblia</i> cell proliferation. Furthermore, our study represents a step toward rational drug design for specific anti-giardiasis therapeutic agents.https://www.mdpi.com/1422-0067/24/15/11992template-based protein modelingstructure–function computational analysistarget of rapamycin<i>Giardia lamblia</i> |
| spellingShingle | Patricia L. A. Muñoz-Muñoz Rosa E. Mares-Alejandre Samuel G. Meléndez-López Marco A. Ramos-Ibarra Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach International Journal of Molecular Sciences template-based protein modeling structure–function computational analysis target of rapamycin <i>Giardia lamblia</i> |
| title | Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach |
| title_full | Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach |
| title_fullStr | Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach |
| title_full_unstemmed | Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach |
| title_short | Structural Insights into the <i>Giardia lamblia</i> Target of Rapamycin Homolog: A Bioinformatics Approach |
| title_sort | structural insights into the i giardia lamblia i target of rapamycin homolog a bioinformatics approach |
| topic | template-based protein modeling structure–function computational analysis target of rapamycin <i>Giardia lamblia</i> |
| url | https://www.mdpi.com/1422-0067/24/15/11992 |
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